title: Mannose receptor and macrophage galactose-type lectin are involved in Bordetella pertussis mast cell interaction.
abstract: Mast cells are crucial in the development of immunity against Bordetella pertussis, and the function of TLRs in this process has been investigated. Here, the interaction between mast cells and B. pertussis with an emphasis on the role of CLRs is examined. In this study, two CLRs, MGL and MR, were detected for the first time on the surface of mast cells. The involvement of MR and MGL in the stimulation of mast cells by heat-inactivated BP was investigated by the use of blocking antibodies and specific carbohydrate ligands. The cell wall LOS of BP was also isolated to explore its role in this interaction. Mast cells stimulated with heat-inactivated BP or BP LOS induced TNF-α, IL-6, and IFN-γ secretion, which was suppressed by blocking MR or MGL. Inhibition of CLRs signaling during BP stimulation affected the ability of mast cells to promote cytokine secretion in T cells but had no effect on the cell-surface expression of ICAM1. Blocking MR or MGL suppressed BP-induced NF-κB expression but not ERK phosphorylation. Syk was involved in the CLR-mediated activation of mast cells by BP. Bacterial recognition by immune cells has been predominantly attributed to TLRs; in this study, the novel role of CLRs in the BP-mast cell interaction is highlighted.
authors.affiliation: Parasite Immune Modulation Group, School of Biotechnology, Faculty of Science and Health, Dublin City University, Glasnevin, Dublin, Ireland.
authors.forename: Krisztina V
authors.initials: KV
authors.lastname: Vukman
authors.forename: Alessandra
authors.initials: A
authors.lastname: Ravidà
authors.forename: Allison M
authors.initials: AM
authors.lastname: Aldridge
authors.forename: Sandra M
authors.initials: SM
authors.lastname: O'Neill
mesh_terms: D000818:Animals; D001212:Asialoglycoproteins / Q000502:physiology*; D001886:Bordetella pertussis / Q000276:immunology*; D004533:Egtazic Acid / Q000494:pharmacology; D018799:Intercellular Adhesion Molecule-1 / Q000032:analysis; D007371:Interferon-gamma / Q000096:biosynthesis; D015850:Interleukin-6 / Q000096:biosynthesis; D047908:Intracellular Signaling Peptides and Proteins / Q000502:physiology; D037181:Lectins, C-Type / Q000502:physiology*; D008070:Lipopolysaccharides / Q000494:pharmacology; D008213:Lymphocyte Activation; D000090323:Mannose Receptor; D037241:Mannose-Binding Lectins / Q000502:physiology*; D008407:Mast Cells / Q000502:physiology*; D008565:Membrane Proteins / Q000502:physiology*; D051379:Mice; D008810:Mice, Inbred C57BL; D016328:NF-kappa B / Q000378:metabolism; D011505:Protein-Tyrosine Kinases / Q000502:physiology; D011956:Receptors, Cell Surface / Q000502:physiology*; D000072377:Syk Kinase; D013601:T-Lymphocytes / Q000276:immunology; D051193:Toll-Like Receptors / Q000502:physiology; D014409:Tumor Necrosis Factor-alpha / Q000096:biosynthesis
chemical_list: D001212:Asialoglycoproteins; C064720:Clec10a protein, mouse; D015850:Interleukin-6; D047908:Intracellular Signaling Peptides and Proteins; D037181:Lectins, C-Type; D008070:Lipopolysaccharides; D000090323:Mannose Receptor; D037241:Mannose-Binding Lectins; D008565:Membrane Proteins; D016328:NF-kappa B; D011956:Receptors, Cell Surface; D051193:Toll-Like Receptors; D014409:Tumor Necrosis Factor-alpha; C023023:lipid-linked oligosaccharides; D018799:Intercellular Adhesion Molecule-1; D004533:Egtazic Acid; D007371:Interferon-gamma; D011505:Protein-Tyrosine Kinases; D000072377:Syk Kinase; C000606897:Syk protein, mouse
keywords: C-type lectin; ERK; ICAM1; NF-κB; cytokine